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Structure of S. cerevisiae ZIP2:SPO16 complex, C2 form

Analyse Structure of S. cerevisiae ZIP2:SPO16 complex, C2 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BZF
Type: protein
Length: 1,559 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sporulation-specific protein 16; Protein ZIP2
UniProt: P17122, P53061
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 7 distinct chains · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sporulation-specific protein 16	protein	197	55% helix, 15% strand	P17122
B, D	Protein ZIP2	protein	206	45% helix, 20% strand	P53061
C	Sporulation-specific protein 16	protein	197	54% helix, 16% strand	P17122
E	Sporulation-specific protein 16	protein	175	52% helix, 17% strand	P17122
F	Protein ZIP2	protein	204	47% helix, 19% strand	P53061
G	Sporulation-specific protein 16	protein	174	48% helix, 18% strand	P17122
H	Protein ZIP2	protein	200	50% helix, 21% strand	P53061

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	965	0.77	0.79	98	empty
2	182	0.67	0.86	31	empty
3	209	0.66	0.85	35	empty
4	204	0.64	0.84	29	empty
5	421	0.59	0.75	39	empty

Interfaces

8 interfaces between chains.

C–D · 2984 Å² buried · 33 hydrogen bonds · protein-protein
A–B · 2953 Å² buried · 28 hydrogen bonds · protein-protein
E–F · 2492 Å² buried · 23 hydrogen bonds · protein-protein
G–H · 2151 Å² buried · 22 hydrogen bonds · protein-protein
A–E · 1124 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 modified (methylation, nonstandard).

Compared structures

6BZF · Structure of S. cerevisiae Zip2:Spo16 complex, C2 form · the same entry in another collection · chain H against H, TM-score 1.00
P53061 · AlphaFold monomer V2.0 prediction for protein ZIP2 (P53061) · a predicted model of the same protein · chain F against A, TM-score 0.99
P17122 · AlphaFold monomer V2.0 prediction for sporulation-specific protein 16 (P17122) · a predicted model of the same protein · chain G against A, TM-score 0.66

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P17122
Every structure of UniProt P53061
Elsewhere: RCSB PDB 6BZF · PDBe 6BZF · UniProt P17122 · UniProt P53061

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